UniProtKB - P03300 (POLG_POL1M)
Genome polyprotein
Functioni
Caution
Catalytic activityi
- EC:2.7.7.48PROSITE-ProRule annotation
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphate1 PublicationEC:3.6.1.151 Publication
- Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. EC:3.4.22.29
- Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.PROSITE-ProRule annotation EC:3.4.22.28
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 25 | Involved in the interaction with human RTN3By similarity | 1 | |
Active sitei | 901 | For Protease 2A activityBy similarity | 1 | |
Active sitei | 919 | For Protease 2A activityBy similarity | 1 | |
Active sitei | 990 | For Protease 2A activityBy similarity | 1 | |
Active sitei | 1605 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1636 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1712 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2076 | For RdRp activity1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1256 – 1263 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: InterPro
- ion channel activity Source: UniProtKB-KW
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: CACAO
- RNA helicase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- endocytosis involved in viral entry into host cell Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
- positive stranded viral RNA replication Source: UniProtKB
- protein complex oligomerization Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- suppression by virus of host mRNA export from nucleus Source: UniProtKB
- suppression by virus of host RIG-I activity Source: UniProtKB-KW
- suppression by virus of host translation initiation factor activity Source: UniProtKB
- transcription, DNA-templated Source: InterPro
- viral RNA genome replication Source: UniProtKB
- virion assembly Source: UniProtKB
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Protein family/group databases
MEROPSi | C03.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 17 chains: Alternative name(s): VP4-VP2 Alternative name(s): P1A Virion protein 4 Alternative name(s): P1B Virion protein 2 Alternative name(s): P1C Virion protein 3 Alternative name(s): P1D Virion protein 1 Alternative name(s): Picornain 2A Protein 2A Alternative name(s): Protein 3B Short name: P3B Protein 3CD (EC:3.4.22.28) Alternative name(s): 3D polymerase Short name: 3Dpol Protein 3D Short name: 3D |
Organismi | Poliovirus type 1 (strain Mahoney) |
Taxonomic identifieri | 12081 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Picornavirales › Picornaviridae › Enterovirus › Enterovirus C › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion
- Host cytoplasm Curated
- Virion 1 Publication
- Host cytoplasm Curated
- Virion 1 Publication
- Host cytoplasm Curated
- Virion 1 Publication
- Host cytoplasm Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
- Host nucleus 1 Publication
- Host cytoplasm 1 Publication
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 1520 | CytoplasmicSequence analysisAdd BLAST | 1519 | |
Intramembranei | 1521 – 1536 | Sequence analysisAdd BLAST | 16 | |
Topological domaini | 1537 – 2209 | CytoplasmicSequence analysisAdd BLAST | 673 |
GO - Cellular componenti
- host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- host cell nucleus Source: UniProtKB-SubCell
- integral to membrane of host cell Source: UniProtKB-KW
- membrane Source: UniProtKB-KW
- T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
- viral capsid Source: UniProtKB
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 | G → A: 100% loss of myristoylation. Impaired viral assembly. 1 Publication | 1 | |
Mutagenesisi | 3 | A → D: 50% loss of myristoylation. Severe reduction in specific infectivity. 1 Publication | 1 | |
Mutagenesisi | 3 | A → G, L or V: No effect on myristoylation and virus growth. 1 Publication | 1 | |
Mutagenesisi | 3 | A → H: No effect on myristoylation. Severe reduction in specific infectivity. 1 Publication | 1 | |
Mutagenesisi | 264 | H → G: Complete loss of VP0 cleavage. 1 Publication | 1 | |
Mutagenesisi | 264 | H → T: Complete loss of VP0 cleavage. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL5127 |
DrugBanki | DB08014 (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE DB08012 (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE DB08013 (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE DB04137 Guanosine-5'-Triphosphate DB08231 Myristic acid DB03963 S-(Dimethylarsenic)Cysteine DB03203 Sphingosine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostBy similarity | |||
ChainiPRO_0000424686 | 2 – 2209 | Genome polyproteinAdd BLAST | 2208 | |
ChainiPRO_0000424687 | 2 – 881 | P1Add BLAST | 880 | |
ChainiPRO_0000424688 | 2 – 341 | Capsid protein VP0Sequence analysisAdd BLAST | 340 | |
ChainiPRO_0000040080 | 2 – 69 | Capsid protein VP4Sequence analysisAdd BLAST | 68 | |
ChainiPRO_0000040081 | 70 – 341 | Capsid protein VP2Sequence analysisAdd BLAST | 272 | |
ChainiPRO_0000040082 | 342 – 579 | Capsid protein VP3Sequence analysisAdd BLAST | 238 | |
ChainiPRO_0000040083 | 580 – 881 | Capsid protein VP1Sequence analysisAdd BLAST | 302 | |
ChainiPRO_0000424689 | 882 – 1456 | P2Add BLAST | 575 | |
ChainiPRO_0000040084 | 882 – 1030 | Protease 2ASequence analysisAdd BLAST | 149 | |
ChainiPRO_0000040085 | 1031 – 1127 | Protein 2BSequence analysisAdd BLAST | 97 | |
ChainiPRO_0000040086 | 1128 – 1456 | Protein 2CSequence analysisAdd BLAST | 329 | |
ChainiPRO_0000424690 | 1457 – 2209 | P3Add BLAST | 753 | |
ChainiPRO_0000424691 | 1457 – 1565 | Protein 3ABSequence analysisAdd BLAST | 109 | |
ChainiPRO_0000424692 | 1457 – 1543 | Protein 3ASequence analysisAdd BLAST | 87 | |
ChainiPRO_0000040088 | 1544 – 1565 | Viral protein genome-linkedSequence analysisAdd BLAST | 22 | |
ChainiPRO_0000424693 | 1566 – 2209 | Protein 3CDSequence analysisAdd BLAST | 644 | |
ChainiPRO_0000040089 | 1566 – 1747 | Protease 3CSequence analysisAdd BLAST | 182 | |
ChainiPRO_0000040090 | 1748 – 2209 | RNA-directed RNA polymeraseAdd BLAST | 462 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by host3 Publications | 1 | |
Modified residuei | 1546 | O-(5'-phospho-RNA)-tyrosine1 Publication | 1 | |
Modified residuei | 1546 | O-UMP-tyrosine; transient2 Publications | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 69 – 70 | Cleavage; by autolysisSequence analysis | 2 | |
Sitei | 341 – 342 | Cleavage; by Protease 3CSequence analysis | 2 | |
Sitei | 881 – 882 | Cleavage; by Protease 2ASequence analysis | 2 | |
Sitei | 1030 – 1031 | Cleavage; by Protease 3CSequence analysis | 2 | |
Sitei | 1127 – 1128 | Cleavage; by Protease 3CSequence analysis | 2 | |
Sitei | 1456 – 1457 | Cleavage; by Protease 3CSequence analysis | 2 | |
Sitei | 1543 – 1544 | Cleavage; by Protease 3CSequence analysis | 2 | |
Sitei | 1565 – 1566 | Cleavage; by Protease 3CSequence analysis | 2 | |
Sitei | 1748 – 1749 | Cleavage; by Protease 3CSequence analysis | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, Lipoprotein, Myristate, PhosphoproteinProteomic databases
PRIDEi | P03300 |
PTM databases
iPTMneti | P03300 |
Interactioni
Subunit structurei
Capsid protein VP1:
Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid.
Interacts with human PVR.
Interacts with capsid protein VP4 in the mature capsid. Capsid protein VP0:
Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2:
Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid. Capsid protein VP3:
Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid.
Interacts with capsid protein VP4 in the mature capsid. Capsid protein VP4:
Interacts with capsid protein VP1 and capsid protein VP3. Protein 2C:
Interacts with cellular Vimentin/VIM and BECN1; these interactions play important roles in the viral replication (By similarity). Protein 2C:
Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis. Protein 2C:
Interacts with host BECN1 and DHX9 and possibly presents a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases. Protein 2C: N-terminus interacts with human RTN3. This interaction is important for viral replication (By similarity). Protein 3AB:
Interacts with protein 3CD. Protein 3A: Homodimerizes and interacts with host GBF1. Protein 3A:
Interacts with host ACBD3 (PubMed:22258260). Viral protein genome-linked:
Interacts with RNA-directed RNA polymerase. Protein 3CD:
Interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase:
Interacts with Viral protein genome-linked and with protein 3CD.
By similarity8 PublicationsProtein-protein interaction databases
ELMi | P03300 |
IntActi | P03300, 4 interactors |
Chemistry databases
BindingDBi | P03300 |
Structurei
Secondary structure
3D structure databases
SMRi | P03300 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03300 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1232 – 1388 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 157 | |
Domaini | 1566 – 1744 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 179 | |
Domaini | 1975 – 2090 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 116 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 580 – 600 | Amphipatic alpha-helixSequence analysisAdd BLAST | 21 | |
Regioni | 1457 – 1479 | DisorderedAdd BLAST | 23 |
Sequence similaritiesi
Keywords - Domaini
RepeatFamily and domain databases
CDDi | cd00205 rhv_like, 3 hits |
Gene3Di | 1.10.10.870, 1 hit 2.60.120.20, 3 hits |
InterProi | View protein in InterPro IPR000605 Helicase_SF3_ssDNA/RNA_vir IPR014759 Helicase_SF3_ssRNA_vir IPR027417 P-loop_NTPase IPR014838 P3A IPR036203 P3A_soluble_dom IPR000081 Peptidase_C3 IPR000199 Peptidase_C3A/C3B_picornavir IPR009003 Peptidase_S1_PA IPR003138 Pico_P1A IPR002527 Pico_P2B IPR001676 Picornavirus_capsid IPR033703 Rhv-like IPR001205 RNA-dir_pol_C IPR007094 RNA-dir_pol_PSvirus IPR029053 Viral_coat |
Pfami | View protein in Pfam PF08727 P3A, 1 hit PF00548 Peptidase_C3, 1 hit PF02226 Pico_P1A, 1 hit PF00947 Pico_P2A, 1 hit PF01552 Pico_P2B, 1 hit PF00680 RdRP_1, 1 hit PF00073 Rhv, 3 hits PF00910 RNA_helicase, 1 hit |
SUPFAMi | SSF50494 SSF50494, 2 hits SSF52540 SSF52540, 1 hit SSF89043 SSF89043, 1 hit |
PROSITEi | View protein in PROSITE PS51874 PCV_3C_PRO, 1 hit PS50507 RDRP_SSRNA_POS, 1 hit PS51218 SF3_HELICASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP
60 70 80 90 100
SKFTEPIKDV LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS
110 120 130 140 150
VVAYGRWPEY LRDSEANPVD QPTEPDVAAC RFYTLDTVSW TKESRGWWWK
160 170 180 190 200
LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEMC
210 220 230 240 250
LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA RRFCPVDYLL
260 270 280 290 300
GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI
310 320 330 340 350
LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG
360 370 380 390 400
SNQYLTADNF QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA
410 420 430 440 450
TKKNTMEMYR VRLSDKPHTD DPILCLSLSP ASDPRLSHTM LGEILNYYTH
460 470 480 490 500
WAGSLKFTFL FCGFMMATGK LLVSYAPPGA DPPKKRKEAM LGTHVIWDIG
510 520 530 540 550
LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV VPLSTPREMD
560 570 580 590 600
ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
610 620 630 640 650
TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS
660 670 680 690 700
RSESSIESFF ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK
710 720 730 740 750
LEFFTYSRFD MELTFVVTAN FTETNNGHAL NQVYQIMYVP PGAPVPEKWD
760 770 780 790 800
DYTWQTSSNP SIFYTYGTAP ARISVPYVGI SNAYSHFYDG FSKVPLKDQS
810 820 830 840 850
AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL KPKHIRVWCP
860 870 880 890 900
RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY
910 920 930 940 950
HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK
960 970 980 990 1000
YYPVSFVGPT FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV
1010 1020 1030 1040 1050
IGIITAGGEG LVAFSDIRDL YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ
1060 1070 1080 1090 1100
ISDKITELTN MVTSTITEKL LKNLIKIISS LVIITRNYED TTTVLATLAL
1110 1120 1130 1140 1150
LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN AAKGLEWVSN
1160 1170 1180 1190 1200
KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ
1210 1220 1230 1240 1250
EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV
1260 1270 1280 1290 1300
CLLVHGSPGT GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV
1310 1320 1330 1340 1350
IMDDLNQNPD GADMKLFCQM VSTVEFIPPM ASLEEKGILF TSNYVLASTN
1360 1370 1380 1390 1400
SSRISPPTVA HSDALARRFA FDMDIQVMNE YSRDGKLNMA MATEMCKNCH
1410 1420 1430 1440 1450
QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE RNRRSNIGNC
1460 1470 1480 1490 1500
MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
1510 1520 1530 1540 1550
NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP
1560 1570 1580 1590 1600
NKKPNVPTIR TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA
1610 1620 1630 1640 1650
ILPTHASPGE SIVIDGKEVE ILDAKALEDQ AGTNLEITII TLKRNEKFRD
1660 1670 1680 1690 1700
IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP VGAVTEQGYL NLGGRQTART
1710 1720 1730 1740 1750
LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK RSYFTQSQGE
1760 1770 1780 1790 1800
IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
1810 1820 1830 1840 1850
DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY
1860 1870 1880 1890 1900
GTDGLEALDL STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL
1910 1920 1930 1940 1950
PLVTYVKDEL RSKTKVEQGK SRLIEASSLN DSVAMRMAFG NLYAAFHKNP
1960 1970 1980 1990 2000
GVITGSAVGC DPDLFWSKIP VLMEEKLFAF DYTGYDASLS PAWFEALKMV
2010 2020 2030 2040 2050
LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG TSIFNSMINN
2060 2070 2080 2090 2100
LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
2110 2120 2130 2140 2150
TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR
2160 2170 2180 2190 2200
WTKDPRNTQD HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST
LYRRWLDSF
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 242 – 264 | RFCPV…FVFPH → SSARWITSLEMARCWGMPLC SA in CAA24446 (PubMed:6272282).CuratedAdd BLAST | 23 | |
Sequence conflicti | 287 | I → L in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 309 | A → V in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 420 – 422 | DDP → AAS in CAA24446 (PubMed:6272282).Curated | 3 | |
Sequence conflicti | 464 | F → S in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 515 | T → S in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 855 – 856 | AV → QL in CAA24446 (PubMed:6272282).Curated | 2 | |
Sequence conflicti | 972 | A → V in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 985 | A → E in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 1140 – 1141 | NA → QR in CAA24446 (PubMed:6272282).Curated | 2 | |
Sequence conflicti | 1619 | V → A in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 1626 – 1627 | AL → VF in CAA24446 (PubMed:6272282).Curated | 2 | |
Sequence conflicti | 1635 | L → F in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 1682 | G → R in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 1722 – 1730 | VIGMHVGGN → SSGCMLVD in CAA24446 (PubMed:6272282).Curated | 9 | |
Sequence conflicti | 1743 | Y → L in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 1752 | Q → P in CAA24446 (PubMed:6272282).Curated | 1 | |
Sequence conflicti | 1759 – 1760 | EV → DA in CAA24446 (PubMed:6272282).Curated | 2 | |
Sequence conflicti | 1840 | T → I in CAA24446 (PubMed:6272282).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01149 Genomic RNA Translation: CAA24461.1 V01148 Genomic RNA Translation: CAA24446.1 |
PIRi | A03898 GNNY2P A93258 GNNY1P |
RefSeqi | NP_041277.1, NC_002058.3 |
Genome annotation databases
GeneIDi | 919920 |
KEGGi | vg:919920 |
Similar proteinsi
Cross-referencesi
Web resourcesi
Virus Particle ExploreR db Icosahedral capsid structure associated with cellular receptor |
Virus Particle ExploreR db Icosahedral capsid structure associated with cellular receptor |
Virus Particle ExploreR db Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication |
Virus Particle ExploreR db Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication |
Virus Particle ExploreR db Icosahedral empty capsid structure |
Virus Particle ExploreR db Icosahedral capsid structure complexed with R78206 |
Virus Particle ExploreR db Icosahedral capsid structure |
Virus Particle ExploreR db Icosahedral capsid structure of 135S cell entry intermediate |
Virus Particle ExploreR db Icosahedral capsid structure |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01149 Genomic RNA Translation: CAA24461.1 V01148 Genomic RNA Translation: CAA24446.1 |
PIRi | A03898 GNNY2P A93258 GNNY1P |
RefSeqi | NP_041277.1, NC_002058.3 |
3D structure databases
Protein-protein interaction databases
ELMi | P03300 |
IntActi | P03300, 4 interactors |
Chemistry databases
BindingDBi | P03300 |
ChEMBLi | CHEMBL5127 |
DrugBanki | DB08014 (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE DB08012 (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE DB08013 (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE DB04137 Guanosine-5'-Triphosphate DB08231 Myristic acid DB03963 S-(Dimethylarsenic)Cysteine DB03203 Sphingosine |
Protein family/group databases
MEROPSi | C03.001 |
PTM databases
iPTMneti | P03300 |
Proteomic databases
PRIDEi | P03300 |
Protocols and materials databases
ABCDi | P03300 |
Genome annotation databases
GeneIDi | 919920 |
KEGGi | vg:919920 |
Miscellaneous databases
EvolutionaryTracei | P03300 |
Family and domain databases
CDDi | cd00205 rhv_like, 3 hits |
Gene3Di | 1.10.10.870, 1 hit 2.60.120.20, 3 hits |
InterProi | View protein in InterPro IPR000605 Helicase_SF3_ssDNA/RNA_vir IPR014759 Helicase_SF3_ssRNA_vir IPR027417 P-loop_NTPase IPR014838 P3A IPR036203 P3A_soluble_dom IPR000081 Peptidase_C3 IPR000199 Peptidase_C3A/C3B_picornavir IPR009003 Peptidase_S1_PA IPR003138 Pico_P1A IPR002527 Pico_P2B IPR001676 Picornavirus_capsid IPR033703 Rhv-like IPR001205 RNA-dir_pol_C IPR007094 RNA-dir_pol_PSvirus IPR029053 Viral_coat |
Pfami | View protein in Pfam PF08727 P3A, 1 hit PF00548 Peptidase_C3, 1 hit PF02226 Pico_P1A, 1 hit PF00947 Pico_P2A, 1 hit PF01552 Pico_P2B, 1 hit PF00680 RdRP_1, 1 hit PF00073 Rhv, 3 hits PF00910 RNA_helicase, 1 hit |
SUPFAMi | SSF50494 SSF50494, 2 hits SSF52540 SSF52540, 1 hit SSF89043 SSF89043, 1 hit |
PROSITEi | View protein in PROSITE PS51874 PCV_3C_PRO, 1 hit PS50507 RDRP_SSRNA_POS, 1 hit PS51218 SF3_HELICASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_POL1M | |
Accessioni | P03300Primary (citable) accession number: P03300 Secondary accession number(s): P03299 Q89679 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | November 13, 2019 | |
This is version 211 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PDB cross-references
Index of Protein Data Bank (PDB) cross-references